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Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]

 CED3_CAERE              Reviewed;         508 AA.
P45436; E3M6B9;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
30-AUG-2017, sequence version 2.
10-OCT-2018, entry version 92.
RecName: Full=Cell death protein 3;
EC=3.4.22.60 {ECO:0000250|UniProtKB:P42573};
AltName: Full=Caspase ced-3 {ECO:0000305};
Contains:
RecName: Full=Cell death protein 3 subunit p17 {ECO:0000250|UniProtKB:P42573};
Contains:
RecName: Full=Cell death protein 3 subunit p15 {ECO:0000250|UniProtKB:P42573};
Contains:
RecName: Full=Cell death protein 3 subunit p13 {ECO:0000250|UniProtKB:P42573};
Flags: Precursor;
Name=ced-3 {ECO:0000312|EMBL:EFO93085.1};
ORFNames=CRE_10123 {ECO:0000312|EMBL:EFO93085.1};
Caenorhabditis remanei (Caenorhabditis vulgaris).
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=31234 {ECO:0000312|Proteomes:UP000008281};
[1] {ECO:0000312|Proteomes:UP000008281}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PB4641 {ECO:0000312|Proteomes:UP000008281};
Caenorhabditis remanei Sequencing Consortium;
Wilson R.K.;
"PCAP assembly of the Caenorhabditis remanei genome.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Acts as a cysteine protease in controlling programmed
cell death (apoptosis) by proteolytically activating or
inactivating a wide range of substrates. Component of the egl-1,
ced-9, ced-4 and ced-3 apoptotic signaling cascade required for
the initiation of programmed cell death in cells fated to die
during embryonic and postembryonic development. During oogenesis,
required for germline apoptosis downstream of ced-9 and ced-4 but
independently of egl-1. By cleaving and activating ced-8, promotes
phosphatidylserine exposure on the surface of apoptotic cells;
phosphatidylserine is a specific marker only present at the
surface of apoptotic cells and acts as a specific signal for
engulfment. By cleaving and converting dcr-1 into a
deoxyribonuclease (DNase), promotes apoptotic chromosomal DNA
fragmentation. By cleaving mitochondrial fission protein drp-1,
may regulate the removal of mitochondria during apoptosis. During
germline apoptosis, cleaves translation initiation factor ifg-1
(isoform p170) promoting cap-independent translation. During male
tail morphogenesis, promotes apoptosis of the tail-spike cell
downstream of ced-4 but independently of egl-1 and ced-9. By
cleaving cnt-1, prevents the activation of the prosurvival akt-1/2
signaling pathway and thus promotes apoptosis. Downstream of ced-
4, may play a role in sex-specific cell apoptosis by cleaving sex-
determining protein fem-1. May regulate germline apoptosis in
response to DNA damage, probably downstream of let-60/ras and mpk-
1 pathway. Cleaves ced-9 in vitro. Cleaves csp-2 isoform b
resulting in the removal of the propeptide and the generation of
csp-2 subunit p31 in vitro. Independently of its apoptotic role
has additional functions. Probably by cleaving and thereby
activating actin-severing protein gsnl-1, required for the
elimination of transient presynaptic components during larval
development downstream of egl-1, ced-9 and ced-4 pathway. Together
with ain-1, a component of the miRNA-induced-silencing complex
(miRISC), regulates temporal cell fate patterning during larval
development. Acts in cell fate patterning by cleaving
heterochronic protein lin-28, likely promoting its degradation.
Also cleaves heterochronic protein lin-14 and exonuclease disl-2
in vitro. Downstream of calreticulin crt-1 and ced-4 and
independently of egl-1 and ced-9, plays a role in the initial
steps of axonal regrowth following axotomy. Cleaves 14-3-3-like
protein ftt-2, tubulin tbb-2 and calrecticulin crt-1 in vitro.
Plays also a role in resistance to S.typhimurium-mediated
infection. {ECO:0000250|UniProtKB:P42573}.
-!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
position P1 and has a preferred cleavage sequence of Asp-Glu-Val-
Asp-|-. {ECO:0000250|UniProtKB:P42573}.
-!- ACTIVITY REGULATION: Octameric ced-4 activates zymogen
autoprocessing and enhances activity of processed ced-3. Zymogen
autoactivation is inhibited by csp-3. csp-3 has no effect on
active ced-3. Zymogen autoactivation is inhibited by csp-2.
Inhibited by cysteine protease inhibitor iodoacetic acid
(CH3COOI). Inhibited by benzyloxycarbonyl-DEVD-fluoro-methyl
ketone (zDEVD-fmk). Inhibited by benzyloxycarbonyl-VAD-fluoro-
methyl ketone (zVAD-fmk). Not inhibited by N-[N-(L-3-
transcarboxirane-2-carbonyl)-leucyl]-agmatine (E-64) or by the
serine and cysteine protease inhibitor L-1-chloro-3-[4-to-
osylamido]-7-amino-2-heptanone (TLCK).
{ECO:0000250|UniProtKB:P42573}.
-!- SUBUNIT: The active form is probably a heterodimer of the p17
subunit with either the p15 or p13 subunit which are all derived
from the precursor by autocatalysis. Interacts with octameric ced-
4 (two ced-3 zymogens per one ced-4 octamer); the interaction
causes the autoproteolytic cleavage and activation of ced-3.
Processed ced-3 also interacts with ced-4 octamer to form a stable
holoenzyme. Interacts (via large subunit p17) with csp-3; the
interaction prevents ced-3 autoactivation and delays ced-4-induced
ced-3 processing. Interacts (via large subunit p17 or small
subunit p13 or p15) with csp-2; the interaction inhibits ced-3
autoactivation. Interacts (via propeptide) with nucleoporin npp-
14; the interaction tethers ced-3 to the nuclear membrane and
prevents its autoprocessing in absence of ced-4. Interacts with
dct-1. May form a complex composed of ced-3, ced-4 and mac-1.
{ECO:0000250|UniProtKB:P42573}.
-!- SUBCELLULAR LOCATION: Nucleus membrane
{ECO:0000250|UniProtKB:P42573}. Perikaryon
{ECO:0000250|UniProtKB:P42573}. Cell junction, synapse
{ECO:0000250|UniProtKB:P42573}. Mitochondrion
{ECO:0000250|UniProtKB:P42573}. Cytoplasm
{ECO:0000250|UniProtKB:P42573}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:P42573}. Note=Colocalizes with nucleoporin
npp-14 to the perinuclear region in germ cells. Becomes diffused
in the cytoplasm in apoptotic germ cells. Localizes to axonal
mitochondria and synapses of DD motor neurons. Synaptic
localization is dependent on axonal mitochondria.
{ECO:0000250|UniProtKB:P42573}.
-!- DOMAIN: The CARD domain is involved in ced-4 binding.
{ECO:0000250|UniProtKB:P42573}.
-!- PTM: Autocatalytic cleavage removes the propeptide and generates
the catalytic subunit p17 and two non-catalytic subunits p15 and
p13; autoproteolysis is induced by ced-4 oligomer. Cleaved by
caspase csp-1 probably at Asp-146 and Asp-376.
{ECO:0000250|UniProtKB:P42573}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DS268426; EFO93085.1; -; Genomic_DNA.
RefSeq; XP_003108285.1; XM_003108237.1.
ProteinModelPortal; P45436; -.
SMR; P45436; -.
STRING; 31234.CRE10123; -.
MEROPS; C14.002; -.
EnsemblMetazoa; CRE10123; CRE10123; WBGene00062743.
GeneID; 9828818; -.
CTD; 9828818; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
OMA; AIVYKNT; -.
OrthoDB; EOG091G05YD; -.
Proteomes; UP000008281; Unassembled WGS sequence.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
Pfam; PF00619; CARD; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00114; CARD; 1.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
3: Inferred from homology;
Apoptosis; Autocatalytic cleavage; Cell junction; Complete proteome;
Cytoplasm; Hydrolase; Membrane; Mitochondrion; Nucleus; Protease;
Reference proteome; Synapse; Thiol protease; Zymogen.
PROPEP 1 223 {ECO:0000250|UniProtKB:P42573}.
/FTId=PRO_0000441119.
CHAIN 224 376 Cell death protein 3 subunit p17.
{ECO:0000305}.
/FTId=PRO_0000004676.
CHAIN 377 508 Cell death protein 3 subunit p15.
{ECO:0000305}.
/FTId=PRO_0000004677.
CHAIN 392 508 Cell death protein 3 subunit p13.
{ECO:0000305}.
/FTId=PRO_0000441120.
DOMAIN 2 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
REGION 392 407 Required for interaction with ced-4.
{ECO:0000250|UniProtKB:P42573}.
ACT_SITE 317 317 {ECO:0000250|UniProtKB:P29466}.
ACT_SITE 360 360 {ECO:0000250|UniProtKB:P42573}.
SITE 223 224 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P42573}.
SITE 376 377 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P42573}.
SITE 391 392 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P42573}.
SEQUENCE 508 AA; 57415 MW; A635C0D101BD3EA8 CRC64;
MMRQDRRNLL ERNILVFSNK LQSEQILEVL IAKQILNADN GDVINSCRTE RDKRKEIVKA
VQRRGDVAFD AFYDALRDTG HHELAAVLEP LARTIDFITP RDLECPMSPA SHRRSRALSP
STFSSPTRVH RDSVSSVSSF TSTYQDVYTR ARSTSRSSRP LHASDRHNYV SPSNSFQSQP
SSANSSFTGC SSLGYSSSRT RSYSKASAHS QYIFHEEDMN YVDAPTIHRV FDEKTMYRNF
STPRGLCLII NNEHFEQMPT RNGTKADKDN ISNLFRCMGY IVHCKDNLTG RAMMLTIRDF
AKNETHGDSA ILVILSHGEE NVIIGVDDVS VNVHEIYDLL NAANAPRLAN KPKLVFVQAC
RGERRDNGFP VLDSVDGVPA LIRPRGWDKG DGPLFNFLGC VRPQAQQVWR KKPSQADILI
AYATTAQYVS WRNSARGSWF IQAVCEVFSL HAKDMDVVEL LTEVNKKVAC GFQTSQGANI
LKQMPELTSR LLKKFYFWPE DRNRSSAV


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